ID Q2I7M3_HORVV Unreviewed; 1130 AA.
AC Q2I7M3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Phytochrome {ECO:0000256|PIRNR:PIRNR000084};
GN Name=PhyA {ECO:0000313|EMBL:ABB13321.1};
OS Hordeum vulgare subsp. vulgare (Domesticated barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=112509 {ECO:0000313|EMBL:ABB13321.1};
RN [1] {ECO:0000313|EMBL:ABB13321.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16489429; DOI=10.1007/s00122-006-0229-y;
RA Szucs P., Karsai I., von Zitzewitz J., Meszaros K., Cooper L.L., Gu Y.Q.,
RA Chen T.H., Hayes P.M., Skinner J.S.;
RT "Positional relationships between photoperiod response QTL and
RT photoreceptor and vernalization genes in barley.";
RL Theor. Appl. Genet. 112:1277-1285(2006).
RN [2] {ECO:0000313|Proteomes:UP000011116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX PubMed=23075845; DOI=10.1038/nature11543;
RG The International Barley Genome Sequencing Consortium;
RA Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT "A physical, genetic and functional sequence assembly of the barley
RT genome.";
RL Nature 491:711-716(2012).
RN [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0338060.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0338060.1};
RG EnsemblPlants;
RL Submitted (JAN-2022) to UniProtKB.
CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that are
CC reversibly interconvertible by light: the Pr form that absorbs
CC maximally in the red region of the spectrum and the Pfr form that
CC absorbs maximally in the far-red region. Photoconversion of Pr to Pfr
CC induces an array of morphogenic responses, whereas reconversion of Pfr
CC to Pr cancels the induction of those responses. Pfr controls the
CC expression of a number of nuclear genes including those encoding the
CC small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B
CC binding protein, protochlorophyllide reductase, rRNA, etc. It also
CC controls the expression of its own gene(s) in a negative feedback
CC fashion. {ECO:0000256|ARBA:ARBA00002479}.
CC -!- PTM: Contains one covalently linked phytochromobilin chromophore.
CC {ECO:0000256|PIRSR:PIRSR000084-50}.
CC -!- SIMILARITY: Belongs to the phytochrome family.
CC {ECO:0000256|ARBA:ARBA00008235, ECO:0000256|PIRNR:PIRNR000084}.
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DR EMBL; DQ201139; ABB13320.1; -; Genomic_DNA.
DR EMBL; DQ201140; ABB13321.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2I7M3; -.
DR STRING; 112509.Q2I7M3; -.
DR PaxDb; 4513-MLOC_81684-1; -.
DR EnsemblPlants; HORVU.MOREX.r3.4HG0338060.1; HORVU.MOREX.r3.4HG0338060.1; HORVU.MOREX.r3.4HG0338060.
DR Gramene; HORVU.MOREX.r2.4HG0281970.1; HORVU.MOREX.r2.4HG0281970.1; HORVU.MOREX.r2.4HG0281970.
DR Gramene; HORVU.MOREX.r3.4HG0338060.1; HORVU.MOREX.r3.4HG0338060.1; HORVU.MOREX.r3.4HG0338060.
DR eggNOG; ENOG502QRSA; Eukaryota.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000011116; Chromosome 4H.
DR ExpressionAtlas; Q2I7M3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR012129; Phytochrome_A-E.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR47876; OS08G0260000 PROTEIN; 1.
DR PANTHER; PTHR47876:SF3; PHYTOCHROME 1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PIRSF; PIRSF000084; Phytochrome; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRNR:PIRNR000084};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000084};
KW Reference proteome {ECO:0000313|Proteomes:UP000011116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR000084};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR000084}.
FT DOMAIN 218..393
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 619..689
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 752..833
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 903..1123
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="phytochromobilin"
FT /ligand_id="ChEBI:CHEBI:189064"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000084-50"
SQ SEQUENCE 1130 AA; 125293 MW; B81044D9855CBB3B CRC64;
MSSSRPATSS SSRNRQSTQE RMLAQTTLDA ELNAEFEESS DSFDYSKLVE AQRDTPTVLQ
EGRSEKVIAY LQHIQRGKMI QSFGCLLALD EKSFNLIAFS ENAPEMLTTV SHAVPSVDDP
PRLDIGTNVR SLFTEQGATA LHKALGFADV SLLNPILVQC KTSGKPFYAI VHRATGCLVV
DFEPVNPTEF PATAAGALQS YKLAAKAISK IQALPGGSME LLCNTVVKEV FELTGYDRVM
AYKFHEDNHG EVFAEITKPG LEPYLGLHYP ATDIPQAARF LFMKNKVRMI CDVRARTLKV
IEDEALPFDI SLCGSSLRAA HSCHLQYMEN MNSIASLVMA VVVNESEEDD EAESEQPAQQ
QKKKILWGLV VCHHESPRYV PFPLRYACEF LAQVFAVHVN KEFEVQKQLR EKSILRMQTI
LSDMLFKEAS PLTIVSGTPN IMDLIKCDGA ALLYGDKVWR LGNAPTESQI RHIALWLSEV
HMDSTGLSTE SLHDAGYPGA SALGDMVCGI AVAKINSNDI LFWFRSHTAE EIRWGGAKND
PSDQDDSRRM HPRLSFKAFL EVVKMKSLAW SDYEMDAIHS LQLILRGALD DVAKPTGKAS
LDEQIGDLKL DGIAELQAVT SEMVRLMETA TVPILAVDGN GLVNGWNQKA AELTGLRVDD
AIGRHILTLV EESSVPVVQR MLYLALQGKE EKEVRFDMKT HGPKRDDGPV ILVVNACASR
DLHDDVVGVC FVAQDMTVHK LVMDKFTRVK GDYMAIVHNP NPLIPPIFGA DEFGWCSEWN
AAMTKLTGWH REEVLDKMLL GEVFDSSNAS CLLKNKDAFV GLCVLINSAL AGEETEKAPF
GFFDRSGKYT ECLLSVNSRA NEDGLITGVF CFIHIPSHEL QQALQVQQAS EQASLRRLKA
FSYMRHAINN PLSGMLYSRK ALKNTDLNEE QMRQIHVSDN CHHQLNKILA DLDQDNIMEN
SSCLDLEMAE FVLQDVVVAA VSQVLIACQG KGIRISCNLP ERFMKQLVYG DGVRLQQILS
DFLSISVKFS PVGGSVEISA QATKNSIGEN LHLIDLELRI KHRGLGVPAE LMAQMFEEEN
TEQSEEGLGL LVSRNLLRLM NGDVRHLREA GMSIFILTAE LACAPTAMRQ
//
